Development of a fluorescently labeled thermostable DHFR for studying conformational changes associated with inhibitor binding

Keyphrases

• Methylenetetrahydrofolate Reductase (MTHFR) 100%
• Conformational Change 100%
• Inhibitor Binding 100%
• Fluorescently Labeled 100%
• Methotrexate 40%
• Intrinsic Tryptophan Fluorescence 30%
• Fluorophore 20%
• Ligand Binding 20%
• Geobacillus Stearothermophilus 20%
• Temperature Effect 10%
• Mutagenesis 10%
• Protein Structure 10%
• Cysteine 10%
• Escherichia Coli Dihydrofolate Reductase 10%
• Ethyl 10%
• Molecular Environment 10%
• Diethylamino 10%
• Conformational Motions 10%
• Stopped-flow Analysis 10%
• Native State 10%
• Binding Interaction 10%
• Thermal Stability 10%
• Coumarin-3-carboxamide 10%

Immunology and Microbiology

• Methotrexate 100%
• Conformational Transition 100%
• Geobacillus stearothermophilus 50%
• Ligand Binding 50%
• Mutagenesis 25%
• Escherichia coli 25%
• Protein Structure 25%
• Motion 25%
• Temperature Dependence 25%
• Thermostability 25%

Pharmacology, Toxicology and Pharmaceutical Science

• Dihydrofolate Reductase 100%
• Methotrexate 36%
• Tryptophan 27%
• Geobacillus stearothermophilus 18%
• Carboxamide 9%
• Mutagenesis 9%
• Escherichia coli 9%
• Cysteine 9%
• Coumarin 9%
• Thermostability 9%